Reviewed, UniProtKB/Swiss-Prot Q19266 (KPC3_CAEEL)

Names and origin

Protein names

Recommended name:
    Protein kinase C-like 3
    EC=2.7.11.13
Alternative name(s):
    Atypical protein kinase C-3
      Short name=aPKC3

Gene names

Name:	pkc-3
Synonyms:	aPKC
ORF Names:	F09E5.1

Organism

Caenorhabditis elegans [Complete proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	597 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Required for the normal progression of embryogenesis and viability of the organism. Plays an indispensable role in establishing embryonic polarity and in recruiting and maintaining par-6 to the periphery, through interaction with par-3. Required for epithelial cell polarity in the distal spermatheca. Phosphorylates serine residues of num-1. Ref.1 Ref.2 Ref.4 Ref.8
Catalytic activity	ATP + a protein = ADP + a phosphoprotein. Ref.2
Cofactor	Magnesium. Ref.2
Subunit structure	Interaction with par-3 required for the peripheral localization of par-6 and to form a par-3/par-6/pkc-3 complex, which is activated when cdc-42 interacts with par-6. Binds avidly to the phosphotyrosine interaction domain (PID) of a novel pkc-3 adapter protein num-1, which enables tethering and targeting of pkc-3 to the cell periphery. Ref.1 Ref.4 Ref.5 Ref.6 Ref.7
Subcellular location	Cytoplasm. Cytoplasm › cytoskeleton. Note: Targeted and anchored at the apical surface (villi) of intestinal and pharyngeal cells, and in proximity with the cortical actin cytoskeleton that lies under the plasma membrane. Tightly bound to organelles/cytoskeleton in six of the seven developmental stages. Accumulation in cytoplasm is restricted to L1 larvae and adults. Co-localized with par-3 at the anterior cortex of the 1-cell embryo. Ref.1 Ref.2
Tissue specificity	Abundantly expressed in the anterior and posterior pharyngeal bulbs, the pharyngeal-intestinal valve, vulval cells, and a region at the posterior end of the intestine that corresponds to site of co-assembly of the intestinal-rectal valve and anal sphincter, and depressor muscles. Modest expression apparent in four hypodermal cells that provide cuticle and muscle anchorage in the tail. Strong expression observed in discrete patches and spots in vulval cells and in somatic cells of the spermatheca. Transiently coexpressed and colocalized with par-6 and par-3, asymmetrically in the developing somatic gonad, including the spermathecal precursor cells of L4 larvae. Ref.2 Ref.4 Ref.8
Developmental stage	Expressed throughout development, at highest level in the L1 stage and lowest in L3. Peripheral staining pattern in early embryos. The staining in 1-cell embryos is weak and uniform just after the completion of meiosis, but increases in intensity and becomes concentrated at the anterior periphery during pronuclear migration. The peripheral staining becomes restricted to about 50% embryo length during the pronuclear meeting and pronuclear fusion stage. By early anaphase, the staining extends posteriorly beyond the midline of the zygote and covers about 60% of the total length of embryos. In 2- and 4-cell stages, staining is uniform at the periphery of the AB cell, its daughters and the EMS cell, but peripheral staining in P1 and P2 is restricted to the boundaries with other blastomeres. Ref.1 Ref.2
Domain	Residues 212-224 are capable of binding the PID domain of num-1 isoform a and isoform c.
Disruption phenotype	Worms show defects in embryogenesis. Mutant embryos show defects in their polarity and cleavage patterns which disrupt hatching. Ref.1
Sequence similarities	Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily. Contains 1 AGC-kinase C-terminal domain. Contains 1 OPR domain. Contains 1 phorbol-ester/DAG-type zinc finger. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Differentiation Fertilization Gastrulation Gonadal differentiation
Cellular component	Cytoplasm Cytoskeleton
Domain	Phorbol-ester binding Zinc-finger
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding Zinc
Molecular function	Developmental protein Kinase Serine/threonine-protein kinase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	body morphogenesis Inferred from mutant phenotype. Source: WormBase cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW embryonic development ending in birth or egg hatching Inferred from mutant phenotype. Source: WormBase establishment or maintenance of cell polarity Ref.1 Inferred from genetic interaction. Source: UniProtKB gastrulation Inferred from electronic annotation. Source: UniProtKB-KW gonadal mesoderm development Inferred from electronic annotation. Source: UniProtKB-KW hermaphrodite genitalia development Inferred from mutant phenotype. Source: WormBase intracellular signaling cascade Inferred from electronic annotation. Source: InterPro negative regulation of vulval development Inferred from mutant phenotype. Source: WormBase protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro single fertilization Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cortical actin cytoskeleton Ref.2 Inferred from direct assay. Source: UniProtKB plasma membrane Ref.2 Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW diacylglycerol binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein domain specific binding Ref.7 Inferred from physical interaction. Source: UniProtKB protein kinase C activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
num-1	Q9XTY6	3	EBI-319158,EBI-495781
num-1	Q9XTY6-1	5	EBI-319158,EBI-495798
par-3	Q17353	2	EBI-319158,EBI-321762
par-6	Q9NAN2	1	EBI-319158,EBI-318782

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 597	597	Protein kinase C-like 3		PRO_0000055737
Regions
	Domain	12 – 95	84	OPR
	Domain	253 – 522	270	Protein kinase
	Domain	524 – 595	72	AGC-kinase C-terminal
	Zinc finger	127 – 177	51	Phorbol-ester/DAG-type
	Nucleotide binding	259 – 267	9	ATP By similarity UniProtKB P41743
Sites
	Active site	377	1	Proton acceptor By similarity UniProtKB P41743
	Binding site	282	1	ATP By similarity UniProtKB P41743
Experimental info
	Mutagenesis	214	1	I → A: Prevents binding with num-1 (isoform a and isoform c). Ref.7
	Mutagenesis	216	1	N → A: Prevents binding with num-1 (isoform a and isoform c). Ref.7
	Mutagenesis	219	1	F → A: Prevents binding with num-1 (isoform a and isoform c). Ref.7
	Mutagenesis	222	1	H → A: No effect on binding with num-1 (isoform a and isoform c). Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Q19266-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: A92760E880DB11B8	FASTA	597	68,035
	10 20 30 40 50 60 MSSPTSLEED GDIKLKTRFQ GQVVVLYARP PLILDDFFAL LKDACKQHKK QDITVKWIDE 70 80 90 100 110 120 DGDPISIDSQ MELDEAVRCL NSSQEAELNI HVFVGKPELP GLPCQGEDKT VYRRGARRWK 130 140 150 160 170 180 KIYLYNGHRF QAKRLNRRIQ CFICHDYIWG IGRQGFRCVD CRLCVHKKCH RHVRTHCGQA 190 200 210 220 230 240 LQGPNIIPMA PASGSLKGAR SNTSSSTTRS GGGIDNGAFH EHEIESPGST SHDASRAMNG 250 260 270 280 290 300 NGSSKWAVSL NDFRLLTVIG RGSYAKVVQA EHVSTRQIYA IKIIKKEMFN EDEDIDWVQT 310 320 330 340 350 360 EKSVFEAASN YPFLVGLHSC FQTESRLFFV IEFVPGGDLM FHMQQQRKLP EEHARFYSGE 370 380 390 400 410 420 IILALHFLHS RGIIYRDLKL DNVLIDAEGH IKLTDYGMCK ENIKDGDLTS TFCGTPNYIA 430 440 450 460 470 480 PEILRGDEYG FSVDWWALGV LMFEMMAGRS PFDIVGMQNS EENTEDYLFQ IILERQIRIP 490 500 510 520 530 540 RSLSVRASGI LKGFLNKDPT ERLGCKLDIN EGLRDMKEHQ FFRGFIDWEA LEQKAVAPPY 550 560 570 580 590 HPAVESDRDL THFDHQFTDE LPQLSPDNPD VIARIDQSEF DGFEYVNPLQ MSREDSV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Atypical protein kinase C cooperates with PAR-3 to establish embryonic polarity in Caenorhabditis elegans." Tabuse Y., Izumi Y., Piano F., Kemphues K.J., Miwa J., Ohno S. Development 125:3607-3614(1998) [PubMed: 9716526] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH PAR-3, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE. Strain: Bristol N2. Tissue: Embryo.
[2]	"Structure, expression, and properties of an atypical protein kinase C (PKC3) from Caenorhabditis elegans. PKC3 is required for the normal progression of embryogenesis and viability of the organism." Wu S.-L., Staudinger J., Olson E.N., Rubin C.S. J. Biol. Chem. 273:1130-1143(1998) [PubMed: 9422779] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. Strain: Bristol N2.
[3]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2.
[4]	"PAR-6 is a conserved PDZ domain-containing protein that colocalizes with PAR-3 in Caenorhabditis elegans embryos." Hung T.-J., Kemphues K.J. Development 126:127-135(1999) [PubMed: 9834192] [Abstract] Cited for: FUNCTION, INTERACTION WITH PAR-3 AND PAR-6, TISSUE SPECIFICITY. Strain: Bristol N2. Tissue: Embryo.
[5]	"CDC-42 controls early cell polarity and spindle orientation in C. elegans." Gotta M., Abraham M.C., Ahringer J. Curr. Biol. 11:482-488(2001) [PubMed: 11412997] [Abstract] Cited for: INTERACTION WITH CDC-42. Strain: Bristol N2. Tissue: Embryo.
[6]	"A novel adapter protein employs a phosphotyrosine binding domain and exceptionally basic N-terminal domains to capture and localize an atypical protein kinase C: characterization of Caenorhabditis elegans C kinase adapter 1, a protein that avidly binds protein kinase C3." Zhang L., Wu S.-L., Rubin C.S. J. Biol. Chem. 276:10463-10475(2001) [PubMed: 11134024] [Abstract] Cited for: INTERACTION WITH NUM-1. Strain: Bristol N2.
[7]	"Structural properties and mechanisms that govern association of C kinase adapter 1 with protein kinase C3 and the cell periphery." Zhang L., Wu S.-L., Rubin C.S. J. Biol. Chem. 276:10476-10484(2001) [PubMed: 11134025] [Abstract] Cited for: INTERACTION WITH NUM-1, MUTAGENESIS OF ILE-214; ASN-216; PHE-219 AND HIS-222.
[8]	"PAR-3 is required for epithelial cell polarity in the distal spermatheca of C. elegans." Aono S., Legouis R., Hoose W.A., Kemphues K.J. Development 131:2865-2874(2004) [PubMed: 15151982] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB007320 mRNA. Translation: BAF80143.1. AF025666 mRNA. Translation: AAB88885.1. U37429 Genomic DNA. Translation: AAA79341.1.
PIR	T16006.
RefSeq	NP_495011.1.
UniGene	Cel.19483
3D structure databases
HSSP	HSSP built from PDB template 1GZK based on UniProtKB P31751.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:24814N.
IntAct	Q19266. 4 interactions.
STRING	Q19266.
Genome annotation databases
Ensembl	F09E5.1.1; F09E5.1.1; F09E5.1; Caenorhabditis elegans. [Genome view] F09E5.1.2; F09E5.1.2; F09E5.1; Caenorhabditis elegans. [Genome view]
GeneID	173914.
KEGG	cel:F09E5.1.
UCSC	F09E5.1.2. c. elegans.
Organism-specific databases
CTD	173914.
WormBase	WBGene00004034. pkc-3.
WormPep	F09E5.1. CE02604. [WorfDB]
Phylogenomic databases
OMA	CIQCKLL.
Enzyme and pathway databases
BRENDA	2.7.11.13. 672.
Gene expression databases
ArrayExpress	Q19266.
Family and domain databases
InterPro	IPR000961. AGC-kinase_C. IPR020454. DAG/PE_bd. IPR000270. OPR_PB1. IPR015745. PKC. IPR012233. PKC_zeta. IPR017892. Pkinase_C. IPR002219. Prot_Kinase_C-like_PE/DAG_bd. IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. IPR002290. Ser_thr_pkinase. [Graphical view]
PANTHER	PTHR22985:SF86. PKC. 1 hit.
Pfam	PF00130. C1_1. 1 hit. PF00564. PB1. 1 hit. PF00069. Pkinase. 1 hit. PF00433. Pkinase_C. 1 hit. [Graphical view]
PIRSF	PIRSF000554. PKC_zeta. 1 hit.
PRINTS	PR00008. DAGPEDOMAIN.
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00109. C1. 1 hit. SM00666. PB1. 1 hit. SM00133. S_TK_X. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view]
PROSITE	PS51285. AGC_KINASE_CTER. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. PS00479. ZF_DAG_PE_1. 1 hit. PS50081. ZF_DAG_PE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	881643.

Entry information

Entry name

KPC3_CAEEL

Accession

Primary (citable) accession number: Q19266
Secondary accession number(s): A7VJC8

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 31, 2004
Last sequence update:	November 1, 1996
Last modified:	November 3, 2009
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Caenorhabditis annotation project